The biological activity of Endomorphin-1 is examined by the Division of Pharmacology, Peptide Institute, Inc.

The discovery and isolation of a potent and selective agonist for the µ- opiate receptor from brain

More than three opioid-receptor subtypes, termed µ, δ, κ have been reported. The endogenous ligand for δ -receptor is enkephalin, and that for κ -receptor is dynorphin. Although opiate alkaloids morphine is well-known for the µ-selective and potent ligand, endogenous ligand "endogenous morphine" has never reported.

Recently, endogenous agonists for the µ-opiate receptor, were first isolated from bovine brain [Nature, 386, 499 (1997)]. These are endomorphin-1; Tyr-Pro-Trp-Phe-NH2, and endomorphin-2; Tyr-Pro-Phe-Phe-NH2. The isolation of relatively large amounts of endomorphin-1 and endomorphin-2 from human brain cortex has also reported [Peptides, 18, 1635 (1997)]. The immunoreactivity for endomorphin was also detected in rat brain near the µ-opiate receptor containing neurons, but the molecular form of the rat peptide has not yet been elucidated [Peptides, 18, 1641 (1997)]. These observations may be considered to indicate that endomorphin-1 and 2 are common µ-opiate agonists in mammals. In addition to the originally discovered µ-opiate agonistic function, these peptides have been reported to show hypotensive activity and Ca2+ channel current inhibitory activity [Biochem. Biophys. Res. Commun., 235, 567 (1997)]. Endomorphins would be useful for the study of pain perception together with some other biological functions in the body.

About Us

With the special support of Peptide Institute, PeptaNova established a well sorted stock of biologically active peptides, enzyme – substrates, enzyme – inhibitors and peptide antisera, located in the heart of Europe.